噬菌体φX174的A蛋白和A*蛋白对单链DNA的切割
Cleavage of single-stranded DNA by the A and A* proteins of bacteriophage phi X174.
作者信息
Langeveld S A, van Mansfeld A D, de Winter J M, Weisbeek P J
出版信息
Nucleic Acids Res. 1979 Dec 20;7(8):2177-88. doi: 10.1093/nar/7.8.2177.
The purified A protein and A* protein of bacteriophage phi X174 have been tested for endonuclease activity on single stranded viral phi X174 DNA. The A protein (55.000 daltons) nicks single-stranded DNA in the same way and at the same place as it does superhelical RFI DNA, at the origin of DNA replication. The A* protein (37.000 daltons) can cleave the single-stranded viral DNA at many different sites. It has however a strong preference for the origin of replication. Both proteins generate 3'OH ends and blocked 5' termini at the nick site.
已经对噬菌体φX174的纯化A蛋白和A蛋白进行了针对单链病毒φX174 DNA的核酸内切酶活性测试。A蛋白（55,000道尔顿）以与切割超螺旋RFI DNA相同的方式且在相同位置，即在DNA复制起点处切割单链DNA。A蛋白（37,000道尔顿）可在许多不同位点切割单链病毒DNA。然而，它强烈偏好复制起点。两种蛋白在切口位点均产生3'OH末端和封闭的5'末端。
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